5jfc

Structural highlights

Function

[SUDHA_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.^{[1] [2]} [REFERENCE:4] [SUDHB_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.^{[3] [4] [5]}

References

1. ↑ Hagen WR, Silva PJ, Amorim MA, Hagedoorn PL, Wassink H, Haaker H, Robb FT. Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. J Biol Inorg Chem. 2000 Aug;5(4):527-34. PMID:10968624
2. ↑ Ma K, Adams MW. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J Bacteriol. 1994 Nov;176(21):6509-17. PMID:7961401
3. ↑ Hagen WR, Silva PJ, Amorim MA, Hagedoorn PL, Wassink H, Haaker H, Robb FT. Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. J Biol Inorg Chem. 2000 Aug;5(4):527-34. PMID:10968624
4. ↑ Ma K, Adams MW. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J Bacteriol. 1994 Nov;176(21):6509-17. PMID:7961401
5. ↑ Ma K, Adams MW. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J Bacteriol. 1994 Nov;176(21):6509-17. PMID:7961401
6. ↑ Lubner CE, Jennings DP, Mulder DW, Schut GJ, Zadvornyy OA, Hoben JP, Tokmina-Lukaszewska M, Berry L, Nguyen DM, Lipscomb GL, Bothner B, Jones AK, Miller AF, King PW, Adams MWW, Peters JW. Mechanistic insights into energy conservation by flavin-based electron bifurcation. Nat Chem Biol. 2017 Apr 10. doi: 10.1038/nchembio.2348. PMID:28394885 doi:http://dx.doi.org/10.1038/nchembio.2348